Chloroperoxidase-catalyzed amino alcohol oxidation: Substrate specificity and novel strategy for the synthesis of N -Cbz-3-aminopropanal

Abstract

This is the author's version of a work that was accepted for publication in Process biochemistry (Elsevier). Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Masdeu, G. et al. "Chloroperoxidase-catalyzed amino alcohol oxidation: substrate specificity and novel strategy for the synthesis of N-Cbz-3-aminopropanal" in

Hybrid chloroperoxidase‐magnetic nanoparticle clusters: effect of functionalization on biocatalyst performance

“…Reaction performance was based on previously published related work . β‐OH (38 mmol L ‐1 ) was dissolved in 100 mmol L ‐1 sodium acetate buffer pH 5.0 in a final volume of 0.7 mL.…”

“…Reaction performance was based on previously published related work. 20 -OH (38 mmol L -1 ) was dissolved in 100 mmol L -1 sodium acetate buffer pH 5.0 in a final volume of 0.7 mL. 0.3 mL mNC-NH 2ox CPO was added with final concentrations of 450 U ox CPO mL -1 , 90 mg mNC mL -1 and 27 mmol L -1 -OH.…”

“…This is the case of chloroperoxidase (CPO, EC 1.11.1.10), a heme‐containing enzyme which catalyzes a wide variety of reactions apart from its natural halogenation . Chloroperoxidase catalyzes alcohol oxidations using peroxides like H 2 O 2 or tert ‐butyl hydroperoxide ( t ‐BuOOH), and it has been recently shown to be able to recognize β‐amino alcohols as substrates . Indeed, cascade bioconversions of β‐amino alcohols oxidation and further aldol addition with dihydroxyacetone catalyzed by d ‐fructose‐6‐phosphate aldolase (FSA, EC 4.1.2) are postulated as an enantioselective biosynthetic route to industrially relevant products, like d ‐fagomine in the case of β‐aminopropanol (β‐OH) .…”

“…[17][18][19] Chloroperoxidase catalyzes alcohol oxidations using peroxides like H 2 O 2 or tert-butyl hydroperoxide (t-BuOOH), and it has been recently shown to be able to recognize -amino alcohols as substrates. 20,21 Indeed, cascade bioconversions of -amino alcohols oxidation and further aldol addition with dihydroxyacetone catalyzed by D-fructose-6-phosphate aldolase (FSA, EC 4.1.2) are postulated as an enantioselective biosynthetic route to industrially relevant products, like D-fagomine in the case of -aminopropanol ( -OH). 22 In these reactions, the major limitations are due to the presence of non-desired secondary reactions and the fast CPO deactivation caused by the required peroxides [23][24][25] or derivate radical species.…”

Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase

“…Another factor that contribute to the stereoselectivity of the hydroxylation reactions is the condition of In addition, further oxidation of alcohols to aldehydes were observed for CPO-catalyzed hydroxylation reactions [120,121]. For example, CPO can catalyze the oxidation of amino alcohol during the synthesis of N-Cbz-3-aminopropanal [122]. The versatility of CPO illustrated the potential of this biocatalyst for practical applications; however, the mechanisms for these reactions are still in controversial.…”